Proceedings of the National Academy of Sciences · 1999 · 226 citations · 24 references
Clot FormationPathologyElectron MicroscopyHematologyCrayfish BloodFish ImmunologyProteomicsProtein FunctionBiochemistryVascular BiologyCrayfish Clotting ProteinBiologyThrombopoiesisNatural SciencesPathogenesisPhysiologyCrustacean BloodHemostasisProtein EngineeringCoagulopathyLipoprotein MetabolismMedicineCrayfish Plasma
Coagulation in crayfish blood is based on the transglutaminase-mediated crosslinking of a specific plasma clotting protein. Here we report the cloning of the subunit of this clotting protein from a crayfish hepatopancreas cDNA library. The ORF encodes a protein of 1,721 amino acids, including a signal peptide of 15 amino acids. Sequence analysis reveals that the clotting protein is homologous to vitellogenins, which are proteins found in vitellogenic females of egg-laying animals. The clotting protein and vitellogenins are all lipoproteins and share a limited sequence similarity to certain other lipoproteins (e.g., mammalian apolipoprotein B and microsomal triglyceride transfer protein) and contain a stretch with similarity to the D domain of mammalian von Willebrand factor. The crayfish clotting protein is present in both sexes, unlike the female-specific vitellogenins. Electron microscopy was used to visualize individual clotting protein molecules and to study the transglutaminase-mediated clotting reaction. In the presence of an endogenous transglutaminase, the purified clotting protein molecules rapidly assemble into long, flexible chains that occasionally branch.
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Basic local alignment search tool
Stephen F. Altschul, Warren Gish, Webb Miller et al. · Journal of Molecular Biology · 1990 · 92.8K citations
Molecular cloning: A laboratory manual
Prescott L. Deininger · Analytical Biochemistry · 1990 · 86.2K citations